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Crystal structure of bat MHC class I ptal-N*01:01 for 2.2 ångström

Analyse Crystal structure of bat MHC class I ptal-N*01:01 for 2.2 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ILC
Type: protein
Length: 385 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MHC class I antigen; Beta-2-microglobulin; Hev-1
UniProt: A0A125R585
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 20% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MHC class I antigen	protein	279	28% helix, 40% strand	A0A125R585
B	Beta-2-microglobulin	protein	98	0% helix, 52% strand	—
C	Hev-1	protein	8	0% helix, 0% strand	—

Pockets

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	516	0.67	0.78	48	empty
2	73	0.49	0.83	17	empty
3	90	0.44	0.79	15	empty
4	69	0.33	0.76	13	empty
5	52	0.28	0.75	14	empty

Interfaces

2 interfaces between chains.

A–B · 1263 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 909 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6ILC · Crystal structure of bat MHC class I ptal-N*01:01 for 2.2 ångström · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A125R585
Elsewhere: RCSB PDB 6ILC · PDBe 6ILC · UniProt A0A125R585

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